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Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP
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| Zeitschriftentitel: | RNA |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | RNA, 12, 2006, 6, S. 1023-1037 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
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| Schlagwörter: |
| author_facet |
Xiao, Shaohua Hsieh, John Nugent, Rebecca L. Coughlin, Daniel J. Fierke, Carol A. Engelke, David R. Xiao, Shaohua Hsieh, John Nugent, Rebecca L. Coughlin, Daniel J. Fierke, Carol A. Engelke, David R. |
|---|---|
| author |
Xiao, Shaohua Hsieh, John Nugent, Rebecca L. Coughlin, Daniel J. Fierke, Carol A. Engelke, David R. |
| spellingShingle |
Xiao, Shaohua Hsieh, John Nugent, Rebecca L. Coughlin, Daniel J. Fierke, Carol A. Engelke, David R. RNA Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP Molecular Biology |
| author_sort |
xiao, shaohua |
| spelling |
Xiao, Shaohua Hsieh, John Nugent, Rebecca L. Coughlin, Daniel J. Fierke, Carol A. Engelke, David R. 1355-8382 1469-9001 Cold Spring Harbor Laboratory Molecular Biology http://dx.doi.org/10.1261/rna.23206 <jats:p>RNase P and RNase MRP are ribonucleoprotein enzymes required for 5′-end maturation of precursor tRNAs (pre-tRNAs) and processing of precursor ribosomal RNAs, respectively. In yeast, RNase P and MRP holoenzymes have eight protein subunits in common, with Pop1p being the largest at >100 kDa. Little is known about the functions of Pop1p, beyond the fact that it binds specifically to the RNase P RNA subunit, <jats:italic>RPR1</jats:italic> RNA. In this study, we refined the previous Pop1 phylogenetic sequence alignment and found four conserved regions. Highly conserved amino acids in yeast Pop1p were mutagenized by randomization and conditionally defective mutations were obtained. Effects of the Pop1p mutations on pre-tRNA processing, pre-rRNA processing, and stability of the RNA subunits of RNase P and MRP were examined. In most cases, functional defects in RNase P and RNase MRP in vivo were consistent with assembly defects of the holoenzymes, although moderate kinetic defects in RNase P were also observed. Most mutations affected both pre-tRNA and pre-rRNA processing, but a few mutations preferentially interfered with only RNase P or only RNase MRP. In addition, one temperature-sensitive mutation had no effect on either tRNA or rRNA processing, consistent with an additional role for RNase P, RNase MRP, or Pop1p in some other form. This study shows that the Pop1p subunit plays multiple roles in the assembly and function of of RNases P and MRP, and that the functions can be differentiated through the mutations in conserved residues.</jats:p> Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP RNA |
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10.1261/rna.23206 |
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Online Free |
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Biologie |
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DE-Rs1 DE-Pl11 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 |
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Cold Spring Harbor Laboratory, 2006 |
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Cold Spring Harbor Laboratory, 2006 |
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1355-8382 1469-9001 |
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| title |
Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_unstemmed |
Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_full |
Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_fullStr |
Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_full_unstemmed |
Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_short |
Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_sort |
functional characterization of the conserved amino acids in pop1p, the largest common protein subunit of yeast rnases p and mrp |
| topic |
Molecular Biology |
| url |
http://dx.doi.org/10.1261/rna.23206 |
| publishDate |
2006 |
| physical |
1023-1037 |
| description |
<jats:p>RNase P and RNase MRP are ribonucleoprotein enzymes required for 5′-end maturation of precursor tRNAs (pre-tRNAs) and processing of precursor ribosomal RNAs, respectively. In yeast, RNase P and MRP holoenzymes have eight protein subunits in common, with Pop1p being the largest at >100 kDa. Little is known about the functions of Pop1p, beyond the fact that it binds specifically to the RNase P RNA subunit, <jats:italic>RPR1</jats:italic> RNA. In this study, we refined the previous Pop1 phylogenetic sequence alignment and found four conserved regions. Highly conserved amino acids in yeast Pop1p were mutagenized by randomization and conditionally defective mutations were obtained. Effects of the Pop1p mutations on pre-tRNA processing, pre-rRNA processing, and stability of the RNA subunits of RNase P and MRP were examined. In most cases, functional defects in RNase P and RNase MRP in vivo were consistent with assembly defects of the holoenzymes, although moderate kinetic defects in RNase P were also observed. Most mutations affected both pre-tRNA and pre-rRNA processing, but a few mutations preferentially interfered with only RNase P or only RNase MRP. In addition, one temperature-sensitive mutation had no effect on either tRNA or rRNA processing, consistent with an additional role for RNase P, RNase MRP, or Pop1p in some other form. This study shows that the Pop1p subunit plays multiple roles in the assembly and function of of RNases P and MRP, and that the functions can be differentiated through the mutations in conserved residues.</jats:p> |
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| author | Xiao, Shaohua, Hsieh, John, Nugent, Rebecca L., Coughlin, Daniel J., Fierke, Carol A., Engelke, David R. |
| author_facet | Xiao, Shaohua, Hsieh, John, Nugent, Rebecca L., Coughlin, Daniel J., Fierke, Carol A., Engelke, David R., Xiao, Shaohua, Hsieh, John, Nugent, Rebecca L., Coughlin, Daniel J., Fierke, Carol A., Engelke, David R. |
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| description | <jats:p>RNase P and RNase MRP are ribonucleoprotein enzymes required for 5′-end maturation of precursor tRNAs (pre-tRNAs) and processing of precursor ribosomal RNAs, respectively. In yeast, RNase P and MRP holoenzymes have eight protein subunits in common, with Pop1p being the largest at >100 kDa. Little is known about the functions of Pop1p, beyond the fact that it binds specifically to the RNase P RNA subunit, <jats:italic>RPR1</jats:italic> RNA. In this study, we refined the previous Pop1 phylogenetic sequence alignment and found four conserved regions. Highly conserved amino acids in yeast Pop1p were mutagenized by randomization and conditionally defective mutations were obtained. Effects of the Pop1p mutations on pre-tRNA processing, pre-rRNA processing, and stability of the RNA subunits of RNase P and MRP were examined. In most cases, functional defects in RNase P and RNase MRP in vivo were consistent with assembly defects of the holoenzymes, although moderate kinetic defects in RNase P were also observed. Most mutations affected both pre-tRNA and pre-rRNA processing, but a few mutations preferentially interfered with only RNase P or only RNase MRP. In addition, one temperature-sensitive mutation had no effect on either tRNA or rRNA processing, consistent with an additional role for RNase P, RNase MRP, or Pop1p in some other form. This study shows that the Pop1p subunit plays multiple roles in the assembly and function of of RNases P and MRP, and that the functions can be differentiated through the mutations in conserved residues.</jats:p> |
| doi_str_mv | 10.1261/rna.23206 |
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| imprint | Cold Spring Harbor Laboratory, 2006 |
| imprint_str_mv | Cold Spring Harbor Laboratory, 2006 |
| institution | DE-Rs1, DE-Pl11, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15 |
| issn | 1355-8382, 1469-9001 |
| issn_str_mv | 1355-8382, 1469-9001 |
| language | English |
| last_indexed | 2024-03-01T16:44:19.449Z |
| match_str | xiao2006functionalcharacterizationoftheconservedaminoacidsinpop1pthelargestcommonproteinsubunitofyeastrnasespandmrp |
| mega_collection | Cold Spring Harbor Laboratory (CrossRef) |
| physical | 1023-1037 |
| publishDate | 2006 |
| publishDateSort | 2006 |
| publisher | Cold Spring Harbor Laboratory |
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| series | RNA |
| source_id | 49 |
| spelling | Xiao, Shaohua Hsieh, John Nugent, Rebecca L. Coughlin, Daniel J. Fierke, Carol A. Engelke, David R. 1355-8382 1469-9001 Cold Spring Harbor Laboratory Molecular Biology http://dx.doi.org/10.1261/rna.23206 <jats:p>RNase P and RNase MRP are ribonucleoprotein enzymes required for 5′-end maturation of precursor tRNAs (pre-tRNAs) and processing of precursor ribosomal RNAs, respectively. In yeast, RNase P and MRP holoenzymes have eight protein subunits in common, with Pop1p being the largest at >100 kDa. Little is known about the functions of Pop1p, beyond the fact that it binds specifically to the RNase P RNA subunit, <jats:italic>RPR1</jats:italic> RNA. In this study, we refined the previous Pop1 phylogenetic sequence alignment and found four conserved regions. Highly conserved amino acids in yeast Pop1p were mutagenized by randomization and conditionally defective mutations were obtained. Effects of the Pop1p mutations on pre-tRNA processing, pre-rRNA processing, and stability of the RNA subunits of RNase P and MRP were examined. In most cases, functional defects in RNase P and RNase MRP in vivo were consistent with assembly defects of the holoenzymes, although moderate kinetic defects in RNase P were also observed. Most mutations affected both pre-tRNA and pre-rRNA processing, but a few mutations preferentially interfered with only RNase P or only RNase MRP. In addition, one temperature-sensitive mutation had no effect on either tRNA or rRNA processing, consistent with an additional role for RNase P, RNase MRP, or Pop1p in some other form. This study shows that the Pop1p subunit plays multiple roles in the assembly and function of of RNases P and MRP, and that the functions can be differentiated through the mutations in conserved residues.</jats:p> Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP RNA |
| spellingShingle | Xiao, Shaohua, Hsieh, John, Nugent, Rebecca L., Coughlin, Daniel J., Fierke, Carol A., Engelke, David R., RNA, Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP, Molecular Biology |
| title | Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_full | Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_fullStr | Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_full_unstemmed | Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_short | Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| title_sort | functional characterization of the conserved amino acids in pop1p, the largest common protein subunit of yeast rnases p and mrp |
| title_unstemmed | Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP |
| topic | Molecular Biology |
| url | http://dx.doi.org/10.1261/rna.23206 |